Chryseobacterium aquifrigidense keratinase liberated essential and nonessential amino acids from chicken feather degradation

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dc.contributor.authorBokveld, Amahle
dc.contributor.authorNnolim, Nonso E.
dc.contributor.authorDigban, Tennison O.
dc.contributor.authorNwodo, Uchechukwu U.
dc.date.accessioned2025-10-14T11:01:58Z
dc.date.available2025-10-14T11:01:58Z
dc.date.issued2023
dc.description.abstractKeratinous biomass valorization for value-added products presents a high prospect in ecological management and the advancement of the bio-economy. Consequently, soil samples from the poultry dumpsite were collected. The bacteria isolated on the basal salt medium were screened for keratinolytic activity. The potent chicken feathers degrading bacteria were identified through 16S rRNA gene sequencing and phylogenetic analysis. Fermentation process conditions were optimized, and the amino acid compositions of the feather hydrolysate were likewise quantified. Ten (10) proteolytic bacteria evaluated on skimmed milk agar showed intact chicken feather degradation ranging from 33% (WDS-03) to 88% (FPS-09). The extracellular keratinase activity ranged from 224.52 ± 42.46 U/mL (WDS-03) to 834.55 ± 66.86 U/mL (FPS-07). Based on 16S rRNA gene sequencing and phylogenetic analysis, the most potent keratinolytic isolates coded as FPS-07, FPS-09, FPS-01, and WDS-06 were identified as Chryseobacterium aquifrigidense FANN1, Chryseobacterium aquifrigidense FANN2, Stenotrophomonas maltophilia ANNb, and Bacillus sp. ANNa, respectively. C aquifrigidense FANN2 maximally produced keratinase (1460.90 ± 26.99 U/mL) at 72 h of incubation under optimal process conditions of pH (6), inoculum side (5%; v/v), temperature (30°C), and chicken feather (25 g/L). The feather hydrolysate showed a protein value of 67.54%, with a relative abundance of arginine (2.84%), serine (3.14%), aspartic acid (3.33%), glutamic acid (3.73%), and glycine (2.81%). C. aquifrigidense FANN2 yielded high keratinase titre and dismembered chicken feathers into amino acids-rich hydrolysate, highlighting its significance in the beneficiation of recalcitrant keratinous wastes into dietary proteins as potential livestock feed supplements.
dc.description.sponsorshipDepartment of Science and Innovation (DSI), and the Technology Innovation Agency (TIA), South Africa, under SIIP enzyme and microbial technologies (grant number: DST/CON/0177/2018).
dc.identifier.citationBokveld, A., Nnolim, N. E., Digban, T. O., Okoh, A. I., & Nwodo, U. U. (2023). Chryseobacterium aquifrigidense keratinase liberated essential and nonessential amino acids from chicken feather degradation. Environmental Technology, 44(3), 293-303. https://doi.org/10.1080/09593330.2021.1969597
dc.identifier.issn1479-487X
dc.identifier.urihttp://hdl.handle.net/20.500.11837/3271
dc.language.isoen
dc.publisherTaylor and Francis
dc.subjectKeratinase
dc.subjectBio-recycling
dc.subjectKeratinous Biomass
dc.subjectAmino Acids
dc.subjectProtein Hydrolysate
dc.titleChryseobacterium aquifrigidense keratinase liberated essential and nonessential amino acids from chicken feather degradation
dc.typeArticle
person.identifier.orcidBokveld, Amahle 0000-0003-2895-6672
person.identifier.orcidNnolim, Nonso E. 0000-0002-7127-7707
person.identifier.orcidDigban, Tennison O. 0000-0002-4604-0556
person.identifier.orcidNwodo, Uchechukwu U. 0000-0003-0646-4028

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